TRPA_PYRFU
ID TRPA_PYRFU Reviewed; 248 AA.
AC Q8U094;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Tryptophan synthase alpha chain {ECO:0000255|HAMAP-Rule:MF_00131};
DE EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00131};
GN Name=trpA {ECO:0000255|HAMAP-Rule:MF_00131}; OrderedLocusNames=PF1705;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=12435500; DOI=10.1111/j.1574-6968.2002.tb11433.x;
RA Ishida M., Oshima T., Yutani K.;
RT "Overexpression in Escherichia coli of the AT-rich trpA and trpB genes from
RT the hyperthermophilic archaeon Pyrococcus furiosus.";
RL FEMS Microbiol. Lett. 216:179-183(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RT "Structures of mutant tryptophan synthase alpha-subunits from a
RT hyperthermophile, Pyrococcus furiosus.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage of
CC indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-
CC glyceraldehyde 3-phosphate + H2O + L-tryptophan;
CC Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00131};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
CC -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
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DR EMBL; AB080770; BAC11856.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81829.1; -; Genomic_DNA.
DR RefSeq; WP_011012851.1; NC_018092.1.
DR PDB; 1GEQ; X-ray; 2.00 A; A/B=1-248.
DR PDB; 1WDW; X-ray; 3.00 A; A/C/E/G/I/K=1-248.
DR PDB; 2DZP; X-ray; 2.40 A; A/B=1-248.
DR PDB; 2DZS; X-ray; 2.40 A; A/B=1-248.
DR PDB; 2DZT; X-ray; 2.40 A; A/B=1-248.
DR PDB; 2DZU; X-ray; 2.46 A; A/B=1-248.
DR PDB; 2DZV; X-ray; 2.40 A; A/B=1-248.
DR PDB; 2DZW; X-ray; 2.40 A; A/B=1-248.
DR PDB; 2DZX; X-ray; 2.40 A; A/B=1-248.
DR PDB; 2E09; X-ray; 2.40 A; A/B=1-248.
DR PDB; 5E0K; X-ray; 2.76 A; A/C/E/G/I/K=1-248.
DR PDBsum; 1GEQ; -.
DR PDBsum; 1WDW; -.
DR PDBsum; 2DZP; -.
DR PDBsum; 2DZS; -.
DR PDBsum; 2DZT; -.
DR PDBsum; 2DZU; -.
DR PDBsum; 2DZV; -.
DR PDBsum; 2DZW; -.
DR PDBsum; 2DZX; -.
DR PDBsum; 2E09; -.
DR PDBsum; 5E0K; -.
DR AlphaFoldDB; Q8U094; -.
DR SMR; Q8U094; -.
DR STRING; 186497.PF1705; -.
DR EnsemblBacteria; AAL81829; AAL81829; PF1705.
DR GeneID; 41713536; -.
DR KEGG; pfu:PF1705; -.
DR PATRIC; fig|186497.12.peg.1773; -.
DR eggNOG; arCOG01086; Archaea.
DR HOGENOM; CLU_016734_0_2_2; -.
DR OMA; LVMTYWN; -.
DR OrthoDB; 65368at2157; -.
DR PhylomeDB; Q8U094; -.
DR BRENDA; 4.2.1.20; 5243.
DR UniPathway; UPA00035; UER00044.
DR EvolutionaryTrace; Q8U094; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR CDD; cd04724; Tryptophan_synthase_alpha; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00131; Trp_synth_alpha; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR018204; Trp_synthase_alpha_AS.
DR InterPro; IPR002028; Trp_synthase_suA.
DR PANTHER; PTHR43406; PTHR43406; 1.
DR Pfam; PF00290; Trp_syntA; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR00262; trpA; 1.
DR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Direct protein sequencing; Lyase; Reference proteome;
KW Tryptophan biosynthesis.
FT CHAIN 1..248
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_0000098897"
FT ACT_SITE 36
FT /note="Proton acceptor"
FT ACT_SITE 47
FT /note="Proton acceptor"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:1GEQ"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:1GEQ"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:1GEQ"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1GEQ"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:1GEQ"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:1GEQ"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:1GEQ"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:1GEQ"
FT HELIX 97..107
FT /evidence="ECO:0007829|PDB:1GEQ"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1GEQ"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1GEQ"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:1GEQ"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:1GEQ"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:1GEQ"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:1GEQ"
FT HELIX 177..189
FT /evidence="ECO:0007829|PDB:1GEQ"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:1GEQ"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:1GEQ"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:1GEQ"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:1GEQ"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:1GEQ"
FT HELIX 235..246
FT /evidence="ECO:0007829|PDB:1GEQ"
SQ SEQUENCE 248 AA; 27497 MW; 45D6C877FB8393EE CRC64;
MFKDGSLIPY LTAGDPDKQS TLNFLLALDE YAGAIELGIP FSDPIADGKT IQESHYRALK
NGFKLREAFW IVKEFRRHSS TPIVLMTYYN PIYRAGVRNF LAEAKASGVD GILVVDLPVF
HAKEFTEIAR EEGIKTVFLA APNTPDERLK VIDDMTTGFV YLVSLYGTTG AREEIPKTAY
DLLRRAKRIC RNKVAVGFGV SKREHVVSLL KEGANGVVVG SALVKIIGEK GREATEFLKK
KVEELLGI
